ID   CHLE1_BRALA             Reviewed;         357 AA.
AC   Q95000;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   27-MAR-2024, entry version 75.
DE   RecName: Full=Cholinesterase 1;
DE            EC=3.1.1.8;
DE   Flags: Fragment;
GN   Name=CHE1;
OS   Branchiostoma lanceolatum (Common lancelet) (Amphioxus lanceolatum).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7740;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9062997;
RX   DOI=10.1002/(sici)1097-010x(19970215)277:3<213::aid-jez3>3.0.co;2-r;
RA   Sutherland D., McClellan J.S., Milner D., Soong W., Axon N., Sanders M.,
RA   Hester A., Kao Y.H., Poczatek T., Routt S., Pezzementi L.;
RT   "Two cholinesterase activities and genes are present in amphioxus.";
RL   J. Exp. Zool. 277:213-229(1997).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an acylcholine + H2O = a carboxylate + choline + H(+);
CC         Xref=Rhea:RHEA:21964, ChEBI:CHEBI:15354, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:29067, ChEBI:CHEBI:35287; EC=3.1.1.8;
CC   -!- SIMILARITY: Belongs to the type-B carboxylesterase/lipase family.
CC       {ECO:0000305}.
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DR   EMBL; U74378; AAB18262.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q95000; -.
DR   SMR; Q95000; -.
DR   MEROPS; S09.980; -.
DR   GO; GO:0004104; F:cholinesterase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR002018; CarbesteraseB.
DR   InterPro; IPR019826; Carboxylesterase_B_AS.
DR   InterPro; IPR019819; Carboxylesterase_B_CS.
DR   InterPro; IPR000997; Cholinesterase.
DR   PANTHER; PTHR43918; ACETYLCHOLINESTERASE; 1.
DR   PANTHER; PTHR43918:SF12; ACETYLCHOLINESTERASE 1; 1.
DR   Pfam; PF00135; COesterase; 1.
DR   PRINTS; PR00878; CHOLNESTRASE.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   PROSITE; PS00122; CARBOXYLESTERASE_B_1; 1.
DR   PROSITE; PS00941; CARBOXYLESTERASE_B_2; 1.
PE   3: Inferred from homology;
KW   Disulfide bond; Hydrolase; Serine esterase.
FT   CHAIN           <1..>357
FT                   /note="Cholinesterase 1"
FT                   /id="PRO_0000070289"
FT   ACT_SITE        112
FT                   /note="Acyl-ester intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10039"
FT   ACT_SITE        244
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        357
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000250"
FT   DISULFID        166..179
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         357
SQ   SEQUENCE   357 AA;  39462 MW;  A2CBDE841704DCDF CRC64;
     TPISEDCLYL NVWQPSPAPT GATVLVWIYG GGFFSGTSSL DVYDGRYLAR MEDVVVVSMN
     YRLGALGFLY TGSEAAPGNA GLLDQHLALQ WVQQNIQSFG GDPGKVTIFG ESAGAASVNF
     HMLSPMSRDL FQRAMMHSAS ALAPWAVTPS EQARQRSKAL AIDIGCSADE EDMDVLVACL
     REVSAQTILD HEWNVVDLSD AHFLADIPFP PVKDGRFITE DPAEMYAAGN FKDIDILVGF
     VKDEGNFWLV YGVPGFDKDT DSIIDRETFV GDIVFCHPRL NDITVERTAF EYTDWLHMDQ
     DTMYRDALDS VFGDPFFVCP TMAVGKAHVN HGRTAYVYEF AQVASNLAWP HWMGAMH
//